T. Ramasarma obtained the bachelor degree in Chemistry from Andhra University (1951), post-graduation in Chemical Engineering from the Indian Institute of Science (IISc) (1953) and Ph. D from Bombay University in Biochemistry (1956). Dr. Ramasarma did post-doctoral work at the National Research Council, Saskatoon, Canada (1956-57), and at the Enzyme Institute, University of Wisconsin, Madison, U.S.A. (1957-58). He returned to India and started research career at IISc and had been a faculty member there till his retirement in 1992. He became a Professor in 1972, the Dean of science faculty (1982-84), and the Chairman of the Department of Biochemistry (1986-89). He worked there as CSIR Emeritus Scientist (1992-97) and as INSA Senior Scientist (1997-2002), and continues association with Solid State & Structural Chemistry Unit, IISc as INSA Honorary Scientist. Dr. Ramasarma joined CDFD as a Distinguished Chair in 2004.

In his long distinguished career Dr. Ramasarma had been honoured as a visiting scientist in leading universities and institutes worldwide: Albert Einstein College of Medicine, New York, U.S.A. (1965-66, 1970), St. Louis University School of Medicine, St. Louis, U.S.A.(1966-67), University of Liverpool, U.K. 1971), University of Wisconsin, Madison as Brittingham Visiting Professor (1980), University of Southern California, Los Angeles, U.S.A. (1983), and University of Hyderabad as Jawaharlal Nehru Professor (1995).

Dr. Ramasarma's research during the past five decades contributed significantly to the contemporary progress in the area of biological oxidations. He published over 250 papers in a variety of national and international journals.

• Sarma Memorial Award, Society of Biological Chemists (India) (1977)
• Silver Jubilee Award for Scientific Research, Mysore University (1980)
• Damodaran Memorial Lecture, Kerala University (1988)
• Fellow, Indian National Science Academy (1988)
• Life Sciences Award, Federation of Indian Chamber of Commerce and Industry (1988)
• Prof. S.S. Koppalikar Memorial Endowment Lecture, Kumta, Karnataka (1994)
• Yellapragada SubbaRow Memorial Oration, Sri Venkateswara Institute of Medical Sciences, Tirupati (1995)
• Motlag Endowment Lectures, University of Madras (1997)
• Distinguished Career Award, South Asian Society on Atherosclerosis and Thrombosis, Mumbai (2000)

1. New functions of coenzyme Q: Water-soluble derivative of the lipid-quinone, coenzyme Q with side chain truncated by oxidation promoted relaxation of contracted arterial smooth muscle, much like nitric oxide. This opens potential of soluble forms of Q for alternate function besides well-known electron transport in mitochondria.

2. Cellular thermogenesis: An scheme involving activation of alpha-adrenergic receptor, generation of hydrogen peroxide, release of iron from stores and activation of NADPH-consuming lipid peroxidation is proposed as a heat-producing mechanism. By not involving any effect on ATP synthesis it has advantage over the mechanism dependent on uncoupling protein and proton discharge in mitochondria.

3. Hydrogen peroxide in cellular functions: Regulation of cellular metabolism by oxidative modifications by hydrogen peroxide had been supported by finding of rapid inactivation of several enzymes such as HMG-CoA reductase, glucose oxidase and glyceraldehydes3-phosphate dehydrogenase. Hydrogen peroxide, occurring in small concentrations, seems to act in presence of abundant cellular peroxicidal enzymes such as catalase, by forming a diperoxo-complex with vanadium that is stable to catalase, yet substitutes efficiently in peroxidations.

4. A new oxo-vanadium radical: A cycle of peroxo-vanadium compounds is constructed to explain oxygen consumption and oxidation of a variety of compounds such a NADH, bromide and benzoate. A radical, ú2), was identified as one of the intermediates formed by ESR spectrum that resembles that of hydroxyl radical but not modified by ethanol.

5. Polypeptide backbone in enzyme reactivity: The peptide bond between XG in the Walker loop in F1-ATPase (GXXXXGKT) flips on nucleotide binding and thus seems produces strain on the g-phosphate bond leading to its hydrolysis. This introduced the new concept that the polypeptide backbone has role in enzyme reactivity.

6. Transmembrane domains: Functional roles for transmembrane domains have been recognized in addition to anchoring the protein in the membrane. These short stretches of about 20 residues are conserved only for the hydrophobicity, but not sequence- selective, and have random choice of exon distribution; several domains in one exon, more than one exon for one domain and two exons sharing the triplet of a residue. Their characteristic codon sequence had been identified as having a pyrimidine inas the second letter, (X C/T X)n, which makes prediction of the domains possible from DNA sequence.